Sandbox Reserved 1559: Difference between revisions
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== Structural highlights and structure-function relationships == | == Structural highlights and structure-function relationships == | ||
This protein has a <scene name='82/823083/6ojttriad/1'>Catalytic Triad</scene> which consists of the amino acids Phe-59, Tyr101, and Lys-134. These amino acids play an important role in catalysis for the protein. Lys-134 proved to be the most important amino acid. The basic spacefill view of the entire protein allows for visualization of the different elements in different colors. The elements shown are carbon (Grey), nitrogen (Blue), and oxygen (Red). The <scene name='82/823083/Spacefill/1'>spacefill view</scene> also allows for visualization of different allosteric binding sites. This protein has a <scene name='82/823083/Nsl_ligand/1'>ligand</scene>, called NSL. | This protein has a <scene name='82/823083/6ojttriad/1'>Catalytic Triad</scene> which consists of the amino acids Phe-59, Tyr101, and Lys-134. These amino acids play an important role in catalysis for the protein. Lys-134 proved to be the most important amino acid. The basic spacefill view of the entire protein allows for visualization of the different elements in different colors. The elements shown are carbon (Grey), nitrogen (Blue), and oxygen (Red). The <scene name='82/823083/Spacefill/1'>spacefill view</scene> also allows for visualization of different allosteric binding sites. This protein has a <scene name='82/823083/Nsl_ligand/1'>ligand</scene>, called NSL. The structural fold of LsdA is that of a <scene name='83/830391/Rainbow_7blade_beta_propeller/2'>seven-bladed β-propeller</scene>. The LsdA active site harbors a single Fe2+ ion that resides at the center of the β-propeller. This metal ion is coordinated in a tetragonal pyramidal fashion by four histidines (His-167, His-218, His-282, and His-472) | ||
<scene name='83/830391/Rainbow_7blade_beta_propeller/2'>seven-bladed β-propeller</scene> | |||